2.3.1.8: phosphate acetyltransferase
This is an abbreviated version!
For detailed information about phosphate acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.8
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2.3.1.8
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acetyl-coenzyme
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methanosarcina
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thermophila
-
formate-lyase
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acetobutylicum
-
pta-ack
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acetogenic
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coash
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acka-pta
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2.7.2.1
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phosphoketolase
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acetoin
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acetate-activating
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butyryl-coa
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tyrobutyricum
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substrate-level
-
2,3-butanediol
-
acetate-grown
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acetylphosphate
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sulfoacetaldehyde
-
synthesis
-
biotechnology
-
biofuel production
- 2.3.1.8
-
acetyl-coenzyme
- methanosarcina
- thermophila
- formate-lyase
- acetobutylicum
-
pta-ack
-
acetogenic
- coash
-
acka-pta
-
2.7.2.1
- phosphoketolase
- acetoin
-
acetate-activating
- butyryl-coa
- tyrobutyricum
-
substrate-level
- 2,3-butanediol
-
acetate-grown
- acetylphosphate
- sulfoacetaldehyde
- synthesis
- biotechnology
- biofuel production
Reaction
Synonyms
acetyl-S-CoA: orthophosphate acetyltransferase, acetyltransferase, phosphate, aster yellows witches'-broom phosphotransacetylase-like enzyme, AYWB-PduL, EutD, Moth_0864, Moth_1181, pduL1, pduL2, PGN_1179, phosphate acetyltransferase, phosphoacylase, phosphotransacetylase, phosphotransacetylase EutD, phosphotransacetylase Pta, PTA, Pta-1, Pta-2, PtaII1, PtaII2
ECTree
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Metals Ions
Metals Ions on EC 2.3.1.8 - phosphate acetyltransferase
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K+
KCl
NH4+
Tris
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maximum activity with Tris buffer, with HEPES and MES catalysis is lowered by ca. 15%
additional information
K+
-
enzyme is activated by low concentrations of NH4+, K+ and Na+, sequence of effectiveness: NH4+, K+, Na+
K+
-
rate of arsenolysis increases with increasing potassium or ammonium salt concentration and reaches a maximum rate at 0.02 to 0.03 M salt concentration
K+
-
enzyme is inactive in absence of K+ or NH4+, maximal activation at about 0.02 M
K+
-
K+ or NH4+ at concentration above 10 mM required for maximum activity
NH4+
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enzyme is activated by low concentrations of NH4+, K+ and Na+, sequence of effectiveness: NH4+, K+, Na+
NH4+
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rate of arsenolysis increases with increasing potassium or ammonium salt concentration and reaches a maximum rate at 0.02 to 0.03 M salt concentration
NH4+
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K+ or NH4+ at concentration above 10 mM required for maximum activity, enzyme is inactive in absence of K+ or NH4+, maximal activation at about 0.02 M
additional information
-
no activity with: Fe3+, Zn2+, Mg2+, Co2+, Ni2+, Sn2+, Cu2+, Mo6+, K+, NH4+